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Volumn 20, Issue 1-2, 2015, Pages 1-17

Deacetylation of chromatin and gene expression regulation: A new target for epigenetic therapy

Author keywords

Acetylation; Biomarker; Cancer; Cell death; Chromatin; Epigenetics; HDAC inhibitor; Histone deacetylase

Indexed keywords

BELINOSTAT; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; PANOBINOSTAT; ROMIDEPSIN; TRICHOSTATIN A; VALPROIC ACID; VORINOSTAT; CHROMATIN; HISTONE; ISOENZYME;

EID: 84922762639     PISSN: 08939675     EISSN: 21626448     Source Type: Journal    
DOI: 10.1615/CritRevOncog.2014012463     Document Type: Article
Times cited : (40)

References (80)
  • 1
    • 84863773570 scopus 로고    scopus 로고
    • The epigenotype. 1942
    • Waddington CH. The epigenotype. 1942. Int J Epidemiol. 2012;41(1):10–3.
    • (2012) Int J Epidemiol , vol.41 , Issue.1 , pp. 10-13
    • Waddington, C.H.1
  • 2
    • 33745602221 scopus 로고    scopus 로고
    • The necessity of a human epigenome project
    • Esteller M. The necessity of a human epigenome project. Carcinogenesis. 2006;27(6):1121–5.
    • (2006) Carcinogenesis , vol.27 , Issue.6 , pp. 1121-1125
    • Esteller, M.1
  • 4
    • 76749090671 scopus 로고    scopus 로고
    • Epigenetics and the biological defni-tion of gene x environment interactions
    • Meaney MJ. Epigenetics and the biological defni-tion of gene x environment interactions. Child Dev. 2010;81(1):41–79.
    • (2010) Child Dev , vol.81 , Issue.1 , pp. 41-79
    • Meaney, M.J.1
  • 5
    • 77957970301 scopus 로고    scopus 로고
    • Epigenetic modifications and human disease
    • Portela A, Esteller M. Epigenetic modifications and human disease. Nat Biotechnol. 2010;28(10): 1057–68.
    • (2010) Nat Biotechnol , vol.28 , Issue.10 , pp. 1057-1068
    • Portela, A.1    Esteller, M.2
  • 6
    • 33644872992 scopus 로고    scopus 로고
    • Chromatin control and cancer-drug discovery: Realizing the promise
    • Inche AG, La Tangue NB. Chromatin control and cancer-drug discovery: realizing the promise. Drug Discov Today. 2006;11(3-4):97–109.
    • (2006) Drug Discov Today , vol.11 , Issue.3-4 , pp. 97-109
    • Inche, A.G.1    La Tangue, N.B.2
  • 8
    • 0041347519 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy: Is transcription the primary target?
    • Johnstone RW, Licht JD. Histone deacetylase inhibitors in cancer therapy: is transcription the primary target? Cancer Cell. 2003;4(1):13–8.
    • (2003) Cancer Cell , vol.4 , Issue.1 , pp. 13-18
    • Johnstone, R.W.1    Licht, J.D.2
  • 9
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Bannister AJ, Kouzarides T. Regulation of chromatin by histone modifications. Cell Res. 2011;21(3): 381–95.
    • (2011) Cell Res , vol.21 , Issue.3 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 10
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. The language of covalent histone modifications. Nature. 2000;403(6765):41–5.
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 11
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • Gregoretti IV, Lee YM, Goodson HV. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J Mol Biol. 2004;338(1):17–31.
    • (2004) J Mol Biol , vol.338 , Issue.1 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 12
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: Implications for disease and therapy
    • Haberland M, Montgomery RL, Olson EN. The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat Rev Genet. 2009;10(1):32–42.
    • (2009) Nat Rev Genet , vol.10 , Issue.1 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 13
    • 39749127166 scopus 로고    scopus 로고
    • The Rpd3/Hda1 family oflysinedeacetylases: From bacteria and yeast to mice and men
    • Yang XJ, Seto E. The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men. Nat Rev Mol Cell Biol. 2008;9(3):206-18.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , Issue.3 , pp. 206-218
    • Yang, X.J.1    Seto, E.2
  • 15
    • 70349227061 scopus 로고    scopus 로고
    • Histone deacetylase HDAC1/HDAC2-controlled embryonic development and cell differentiation
    • Brunmeir R, Lagger S, Seiser C. Histone deacetylase HDAC1/HDAC2-controlled embryonic development and cell differentiation. Int J Dev Biol. 2009;53(2-3):275–89.
    • (2009) Int J Dev Biol , vol.53 , Issue.2-3 , pp. 275-289
    • Brunmeir, R.1    Lagger, S.2    Seiser, C.3
  • 16
    • 61549116543 scopus 로고    scopus 로고
    • Histone deacetylases: Salesmen and customers in the post-translational modification market
    • Brandl A, Heinzel T, Kramer OH. Histone deacetylases: salesmen and customers in the post-translational modification market. Biol Cell. 2009;101(4):193–205.
    • (2009) Biol Cell , vol.101 , Issue.4 , pp. 193-205
    • Brandl, A.1    Heinzel, T.2    Kramer, O.H.3
  • 17
    • 67649305191 scopus 로고    scopus 로고
    • Epigenetics in cancer: Targeting chromatin modifications
    • Ellis L, Atadja PW, Johnstone RW. Epigenetics in cancer: targeting chromatin modifications. Mol Cancer Ter. 2009;8(6):1409–20.
    • (2009) Mol Cancer Ter , vol.8 , Issue.6 , pp. 1409-1420
    • Ellis, L.1    Atadja, P.W.2    Johnstone, R.W.3
  • 18
    • 34548526743 scopus 로고    scopus 로고
    • Chromatin remodeling and cancer, Part I: Covalent histone modifications
    • Wang GG, Allis CD, Chi P. Chromatin remodeling and cancer, Part I: covalent histone modifications. Trends Mol Med. 2007;13(9):363–72.
    • (2007) Trends Mol Med , vol.13 , Issue.9 , pp. 363-372
    • Wang, G.G.1    Allis, C.D.2    Chi, P.3
  • 19
    • 40849139208 scopus 로고    scopus 로고
    • Epigenetics in cancer
    • Esteller M. Epigenetics in cancer. New Engl J Med. 2008;358(11):1148–59.
    • (2008) New Engl J Med , vol.358 , Issue.11 , pp. 1148-1159
    • Esteller, M.1
  • 21
    • 84869869682 scopus 로고    scopus 로고
    • HDAC inhibitor-based therapies: Can we interpret the code?
    • New M, Olzscha H, La Tangue NB. HDAC inhibitor-based therapies: can we interpret the code? Mol Oncol. 2012;6(6):637–56.
    • (2012) Mol Oncol , vol.6 , Issue.6 , pp. 637-656
    • New, M.1    Olzscha, H.2    La Tangue, N.B.3
  • 24
    • 74549200467 scopus 로고    scopus 로고
    • Is there a future for histone deacetylase inhibitors in the pharmacotherapy of psychiatric disorders?
    • Grayson DR, Kundakovic M, Sharma RP. Is there a future for histone deacetylase inhibitors in the pharmacotherapy of psychiatric disorders? Mol Pharmacol. 2010;77(2):126–35.
    • (2010) Mol Pharmacol , vol.77 , Issue.2 , pp. 126-135
    • Grayson, D.R.1    Kundakovic, M.2    Sharma, R.P.3
  • 26
    • 0026580006 scopus 로고
    • Brahma: A regulator of Drosophila homeotic genes structurally related to the yeast transcriptional activator SNF2/ SWI2
    • Tamkun JW, Deuring R, Scott MP, Kissinger M, Pattatucci AM, Kaufman TC, Kennison JA. brahma: a regulator of Drosophila homeotic genes structurally related to the yeast transcriptional activator SNF2/ SWI2. Cell. 1992;68(3):561–72.
    • (1992) Cell , vol.68 , Issue.3 , pp. 561-572
    • Tamkun, J.W.1    Deuring, R.2    Scott, M.P.3    Kissinger, M.4    Pattatucci, A.M.5    Kaufman, T.C.6    Kennison, J.A.7
  • 27
    • 55949130820 scopus 로고    scopus 로고
    • Epigenetics of beta-globin gene regulation
    • Kiefer CM, Hou C, Little JA, Dean A. Epigenetics of beta-globin gene regulation. Mutat Res. 2008;647(1-2):68-76.
    • (2008) Mutat Res , vol.647 , Issue.1-2 , pp. 68-76
    • Kiefer, C.M.1    Hou, C.2    Little, J.A.3    Dean, A.4
  • 28
    • 0027525970 scopus 로고
    • Studies of the DNA binding properties of histone H4 amino terminus. Termal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 “tail” to DNA
    • Hong L, Schroth GP, Matthews HR, Yau P, Bradbury EM. Studies of the DNA binding properties of histone H4 amino terminus. Termal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 “tail” to DNA. J Biol Chem. 1993;268(1):305–14.
    • (1993) J Biol Chem , vol.268 , Issue.1 , pp. 305-314
    • Hong, L.1    Schroth, G.P.2    Matthews, H.R.3    Yau, P.4    Bradbury, E.M.5
  • 29
    • 0029123092 scopus 로고
    • Histone H4 and the maintenance of genome integrity
    • Megee PC, Morgan BA, Smith MM. Histone H4 and the maintenance of genome integrity. Genes Dev. 1995;9(14):1716–27.
    • (1995) Genes Dev , vol.9 , Issue.14 , pp. 1716-1727
    • Megee, P.C.1    Morgan, B.A.2    Smith, M.M.3
  • 30
    • 3843103739 scopus 로고    scopus 로고
    • Redundant roles for histone H3 N-terminal lysine residues in subtelomeric gene repression in Saccharomyces cerevisiae
    • Martin AM, Pouchnik DJ, Walker JL, Wyrick JJ. Redundant roles for histone H3 N-terminal lysine residues in subtelomeric gene repression in Saccharomyces cerevisiae. Genetics. 2004;167(3):1123–32.
    • (2004) Genetics , vol.167 , Issue.3 , pp. 1123-1132
    • Martin, A.M.1    Pouchnik, D.J.2    Walker, J.L.3    Wyrick, J.J.4
  • 31
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. Translating the histone code. Science. 2001;293(5532):1074-80.
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 32
    • 0033988813 scopus 로고    scopus 로고
    • DNA methyltransferase Dnmt1 associates with histone deacetylase activity
    • Fuks F, Burgers WA, Brehm A, Hughes-Davies L, Kouzarides T. DNA methyltransferase Dnmt1 associates with histone deacetylase activity. Nat Genet. 2000;24(1):88–91.
    • (2000) Nat Genet , vol.24 , Issue.1 , pp. 88-91
    • Fuks, F.1    Burgers, W.A.2    Brehm, A.3    Hughes-Davies, L.4    Kouzarides, T.5
  • 34
    • 33847070442 scopus 로고    scopus 로고
    • Tse role of chromatin during transcription
    • Li B, Carey M, Workman JL. The role of chromatin during transcription. Cell. 2007;128(4):707–19.
    • (2007) Cell , vol.128 , Issue.4 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 35
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass CK, Rosenfeld MG. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev. 2000;14(2):121–41.
    • (2000) Genes Dev , vol.14 , Issue.2 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 37
    • 0033919595 scopus 로고    scopus 로고
    • DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters
    • Robertson KD, Ait-Si-Ali S, Yokochi T, Wade PA, Jones PL, Wolfe AP. DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters. Nat Genet. 2000;25(3):338–42.
    • (2000) Nat Genet , vol.25 , Issue.3 , pp. 338-342
    • Robertson, K.D.1    Ait-Si-Ali, S.2    Yokochi, T.3    Wade, P.A.4    Jones, P.L.5    Wolfe, A.P.6
  • 38
    • 33645830066 scopus 로고    scopus 로고
    • DNA-damage-responsive acetylation of pRb regulates binding to E2F-1
    • Markham D, Munro S, Soloway J, O’Connor DP, La Tangue NB. DNA-damage-responsive acetylation of pRb regulates binding to E2F-1. EMBO Rep. 2006;7(2):192–8.
    • (2006) EMBO Rep , vol.7 , Issue.2 , pp. 192-198
    • Markham, D.1    Munro, S.2    Soloway, J.3    O’Connor, D.P.4    La Tangue, N.B.5
  • 39
    • 0142123190 scopus 로고    scopus 로고
    • Histone deacetylation of RB-responsive promoters: Requisite for specific gene repression but dispensable for cell cycle inhibition
    • Siddiqui H, Solomon DA, Gunawardena RW, Wang Y, Knudsen ES. Histone deacetylation of RB-responsive promoters: requisite for specific gene repression but dispensable for cell cycle inhibition. Mol Cell Biol. 2003;23(21):7719–31.
    • (2003) Mol Cell Biol , vol.23 , Issue.21 , pp. 7719-7731
    • Siddiqui, H.1    Solomon, D.A.2    Gunawardena, R.W.3    Wang, Y.4    Knudsen, E.S.5
  • 40
    • 0142122363 scopus 로고    scopus 로고
    • Overexpression of histone deacetylase HDAC1 modulates breast cancer progression by negative regulation of estrogen receptor alpha
    • Kawai H, Li H, Avraham S, Jiang S, Avraham HK. Overexpression of histone deacetylase HDAC1 modulates breast cancer progression by negative regulation of estrogen receptor alpha. Int J Cancer. 2003;107(3):353–8.
    • (2003) Int J Cancer , vol.107 , Issue.3 , pp. 353-358
    • Kawai, H.1    Li, H.2    Avraham, S.3    Jiang, S.4    Avraham, H.K.5
  • 41
    • 0018221572 scopus 로고
    • Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
    • Laskey RA, Honda BM, Mills AD, Finch J T. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature. 1978;275(5679):416–20.
    • (1978) Nature , vol.275 , Issue.5679 , pp. 416-420
    • Laskey, R.A.1    Honda, B.M.2    Mills, A.D.3    Finch, J.T.4
  • 42
    • 44949119317 scopus 로고    scopus 로고
    • Histone chaperones in nucleo-some eviction and histone exchange
    • Park YJ, Luger K. Histone chaperones in nucleo-some eviction and histone exchange. Curr Opin Struct Biol. 2008;18(3):282–9.
    • (2008) Curr Opin Struct Biol , vol.18 , Issue.3 , pp. 282-289
    • Park, Y.J.1    Luger, K.2
  • 46
    • 84869874931 scopus 로고    scopus 로고
    • The HAT/ HDAC interplay: Multilevel control of STAT signaling
    • Icardi L, De Bosscher K, Tavernier J. The HAT/ HDAC interplay: multilevel control of STAT signaling. Cytokine Growth Factor Rev. 2012;23(6):283–91.
    • (2012) Cytokine Growth Factor Rev , vol.23 , Issue.6 , pp. 283-291
    • Icardi, L.1    De Bosscher, K.2    Tavernier, J.3
  • 47
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature. 2011;475(7356):324–32.
    • (2011) Nature , vol.475 , Issue.7356 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 48
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali P, Pranpat M, Bradner J, Balasis M, Fiskus W, Guo F, Rocha K, Kumaraswamy S, Boyapalle S, Atadia P, Seto E, Bhalla K. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J Biol Chem. 2005;280(29):26729–34.
    • (2005) J Biol Chem , vol.280 , Issue.29 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3    Balasis, M.4    Fiskus, W.5    Guo, F.6    Rocha, K.7    Kumaraswamy, S.8    Boyapalle, S.9    Atadia, P.10    Seto, E.11    Bhalla, K.12
  • 49
    • 0043016178 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor LAQ824 both lowers expression and promotes proteasomal degradation of Bcr-Abl and induces apoptosis of imatinib mesylate-sensitive or -refractory chronic myelogenous leukemia-blast crisis cells
    • Nimmanapalli R, Fuino L, Bali P, Gasparetto M, Glozak M, Tao J, Moscinski L, Smith C, Wu J, Jove R, Atadia P, Bhalla K. Histone deacetylase inhibitor LAQ824 both lowers expression and promotes proteasomal degradation of Bcr-Abl and induces apoptosis of imatinib mesylate-sensitive or -refractory chronic myelogenous leukemia-blast crisis cells. Cancer Res. 2003;63(16):5126–35.
    • (2003) Cancer Res , vol.63 , Issue.16 , pp. 5126-5135
    • Nimmanapalli, R.1    Fuino, L.2    Bali, P.3    Gasparetto, M.4    Glozak, M.5    Tao, J.6    Moscinski, L.7    Smith, C.8    Wu, J.9    Jove, R.10    Atadia, P.11    Bhalla, K.12
  • 51
    • 84896843332 scopus 로고    scopus 로고
    • Interplay of acetyltransferase EP300 and the proteasome system in regulating heat shock transcription factor 1
    • Raychaudhuri S, Loew C, Korner R, Pinkert S, Theis M, Hayer-Hartl M, Buchholz F, Hartl F U. Interplay of acetyltransferase EP300 and the proteasome system in regulating heat shock transcription factor 1. Cell. 2014;156(5): 975–85.
    • (2014) Cell , vol.156 , Issue.5 , pp. 975-985
    • Raychaudhuri, S.1    Loew, C.2    Korner, R.3    Pinkert, S.4    Theis, M.5    Hayer-Hartl, M.6    Buchholz, F.7    Hartl, F.U.8
  • 53
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon VM, Sandhof TW, Rifkind RA, Marks PA. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc Natl Acad Sci U S A. 2000;97(18):10014–9.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.18 , pp. 10014-10019
    • Richon, V.M.1    Sandhof, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 62
    • 41549159879 scopus 로고    scopus 로고
    • Class I histone deacetylase expression has independent prognostic impact in human colorectal cancer: Specific role of class I histone deacetylases in vitro and in vivo
    • Weichert W, Roske A, Niesporek S, Noske A, Buckendahl AC, Dietel M, Gekeler V, Boehm M, Beckers T, Denkert C. Class I histone deacetylase expression has independent prognostic impact in human colorectal cancer: specific role of class I histone deacetylases in vitro and in vivo. Clin Cancer Res. 2008;14(6):1669–77.
    • (2008) Clin Cancer Res , vol.14 , Issue.6 , pp. 1669-1677
    • Weichert, W.1    Roske, A.2    Niesporek, S.3    Noske, A.4    Buckendahl, A.C.5    Dietel, M.6    Gekeler, V.7    Boehm, M.8    Beckers, T.9    Denkert, C.10
  • 65
    • 56149090684 scopus 로고    scopus 로고
    • Epi-drugs to fight cancer: From chemistry to cancer treatment, the road ahead
    • Mai A, Altucci L. Epi-drugs to fight cancer: from chemistry to cancer treatment, the road ahead. Int J Biochem Cell Biol. 2009;41(1):199–213.
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.1 , pp. 199-213
    • Mai, A.1    Altucci, L.2
  • 66
    • 84901523040 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in glioblastoma: Pre-clinical and clinical experience
    • Bezecny P. Histone deacetylase inhibitors in glioblastoma: pre-clinical and clinical experience. Med Oncol. 2014;31(985).
    • (2014) Med Oncol , vol.31 , Issue.985
    • Bezecny, P.1
  • 67
    • 77955643796 scopus 로고    scopus 로고
    • The clinical development of histone deacetylase inhibitors as targeted anticancer drugs
    • Marks PA. The clinical development of histone deacetylase inhibitors as targeted anticancer drugs. Expert Opin Investig Drugs. 2010;19(9):1049–66.
    • (2010) Expert Opin Investig Drugs , vol.19 , Issue.9 , pp. 1049-1066
    • Marks, P.A.1
  • 68
    • 77955355838 scopus 로고    scopus 로고
    • Rational design and simple chemistry yield a superior, neuroprotective HDAC6 inhibitor, tubastatin A
    • Butler KV, Kalin J, Brochier C, Vistoli G, Langley B, Kozikowski AP. Rational design and simple chemistry yield a superior, neuroprotective HDAC6 inhibitor, tubastatin A. J Am Chem Soc. 2010;132(31):10842–6.
    • (2010) J Am Chem Soc , vol.132 , Issue.31 , pp. 10842-10846
    • Butler, K.V.1    Kalin, J.2    Brochier, C.3    Vistoli, G.4    Langley, B.5    Kozikowski, A.P.6
  • 69
    • 84860390334 scopus 로고    scopus 로고
    • Predictive biomarkers: A paradigm shift towards personalized cancer medicine
    • La Tangue NB, Kerr DJ. Predictive biomarkers: a paradigm shift towards personalized cancer medicine. Nat Rev Clin Oncol. 2011;8(10):587–96.
    • (2011) Nat Rev Clin Oncol , vol.8 , Issue.10 , pp. 587-596
    • La Tangue, N.B.1    Kerr, D.J.2
  • 70
    • 78651361884 scopus 로고    scopus 로고
    • Targeting histone deacetyalses in the treatment of B- and T-cell malignancies
    • Zain J, O’Connor OA. Targeting histone deacetyalses in the treatment of B- and T-cell malignancies. Invest New Drugs. 2010;28 Suppl 1:S58–78.
    • Invest New Drugs. 2010;28 Suppl , vol.1 , pp. S58-S78
    • Zain, J.1    O’Connor, O.A.2
  • 75
    • 84901706232 scopus 로고    scopus 로고
    • Belinostat for the treatment of peripheral T-cell lymphomas
    • McDermott J, Jimeno A. Belinostat for the treatment of peripheral T-cell lymphomas. Drugs Today (Barc). 2014;50(5):337–45.
    • (2014) Drugs Today (Barc) , vol.50 , Issue.5 , pp. 337-345
    • McDermott, J.1    Jimeno, A.2
  • 76
    • 84928774345 scopus 로고    scopus 로고
    • Belinostat: First global approval
    • Poole RM. Belinostat: first global approval. Drugs. 2014;74(13)1543–54.
    • (2014) Drugs , vol.74 , Issue.13 , pp. 1543-1554
    • Poole, R.M.1
  • 77
    • 84891837817 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: An overview of the clinical studies in solid tumors
    • Slingerland M, Guchelaar HJ, Gelderblom H. Histone deacetylase inhibitors: an overview of the clinical studies in solid tumors. Anti-cancer Drugs. 2014;25(2):140–9.
    • (2014) Anti-Cancer Drugs , vol.25 , Issue.2 , pp. 140-149
    • Slingerland, M.1    Guchelaar, H.J.2    Gelderblom, H.3
  • 78
    • 84901987401 scopus 로고    scopus 로고
    • The role of epigenetics in the biology of multiple myeloma
    • Dimopoulos K, Gimsing P, Gronbaek K. The role of epigenetics in the biology of multiple myeloma. Blood Cancer J. 2014;4:e207.
    • (2014) Blood Cancer J , vol.4
    • Dimopoulos, K.1    Gimsing, P.2    Gronbaek, K.3


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